ID   3MGA_BACSU              Reviewed;         303 AA.
AC   P37878;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=DNA-3-methyladenine glycosylase;
DE            EC=3.2.2.21;
DE   AltName: Full=3-methyladenine-DNA glycosidase;
GN   Name=alkA; OrderedLocusNames=BSU01800;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ROLE IN
RP   RESISTANCE TO ALKYLATION DAMAGE, GENE NAME, INDUCTION, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=168;
RX   PubMed=8376346; DOI=10.1128/jb.175.18.6010-6017.1993;
RA   Morohoshi F., Hayashi K., Munakata N.;
RT   "Bacillus subtilis alkA gene encoding inducible 3-methyladenine DNA
RT   glycosylase is adjacent to the ada operon.";
RL   J. Bacteriol. 175:6010-6017(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Haga K., Liu H., Yasumoto K., Takahashi H., Yoshikawa H.;
RT   "Sequence analysis of the 70kb region between 17 and 23 degree of the
RT   Bacillus subtilis chromosome.";
RL   Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
CC   -!- FUNCTION: Is involved in the adaptive response to alkylation damage in
CC       DNA caused by alkylating agents. Catalyzes the hydrolysis of the
CC       deoxyribose N-glycosidic bond to excise 3-methyladenine and 7-
CC       methylguanine from the damaged DNA polymer formed by alkylation
CC       lesions. {ECO:0000269|PubMed:8376346}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of alkylated DNA, releasing 3-methyladenine, 3-
CC         methylguanine, 7-methylguanine and 7-methyladenine.; EC=3.2.2.21;
CC         Evidence={ECO:0000269|PubMed:8376346};
CC   -!- INDUCTION: Up-regulated by methylated AdaA in response to the exposure
CC       to alkylating agents. {ECO:0000269|PubMed:8376346}.
CC   -!- DISRUPTION PHENOTYPE: Disruption of this gene sensitizes cells to the
CC       alkylating agent N-propyl-N'-nitro-N-nitrosoguanidine.
CC       {ECO:0000269|PubMed:8376346}.
CC   -!- MISCELLANEOUS: Overproduction of this gene renders cells highly
CC       resistant to the alkylating agent N-propyl-N'-nitro-N-nitrosoguanidine.
CC   -!- SIMILARITY: Belongs to the alkylbase DNA glycosidase AlkA family.
CC       {ECO:0000305}.
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DR   EMBL; D14465; BAA03361.1; -; Genomic_DNA.
DR   EMBL; AB006424; BAA33073.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11956.1; -; Genomic_DNA.
DR   PIR; E69584; E69584.
DR   RefSeq; NP_388061.1; NC_000964.3.
DR   RefSeq; WP_003234926.1; NZ_JNCM01000030.1.
DR   AlphaFoldDB; P37878; -.
DR   SMR; P37878; -.
DR   STRING; 224308.BSU01800; -.
DR   PaxDb; P37878; -.
DR   PRIDE; P37878; -.
DR   DNASU; 938586; -.
DR   EnsemblBacteria; CAB11956; CAB11956; BSU_01800.
DR   GeneID; 938586; -.
DR   KEGG; bsu:BSU01800; -.
DR   PATRIC; fig|224308.179.peg.186; -.
DR   eggNOG; COG0122; Bacteria.
DR   InParanoid; P37878; -.
DR   OMA; WYIWRSL; -.
DR   PhylomeDB; P37878; -.
DR   BioCyc; BSUB:BSU01800-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0032993; C:protein-DNA complex; IBA:GO_Central.
DR   GO; GO:0032131; F:alkylated DNA binding; IBA:GO_Central.
DR   GO; GO:0008725; F:DNA-3-methyladenine glycosylase activity; IBA:GO_Central.
DR   GO; GO:0052822; F:DNA-3-methylguanine glycosylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052821; F:DNA-7-methyladenine glycosylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0043916; F:DNA-7-methylguanine glycosylase activity; IBA:GO_Central.
DR   GO; GO:0008534; F:oxidized purine nucleobase lesion DNA N-glycosylase activity; IEA:InterPro.
DR   GO; GO:0006285; P:base-excision repair, AP site formation; IBA:GO_Central.
DR   GO; GO:0006307; P:DNA dealkylation involved in DNA repair; IBA:GO_Central.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR   CDD; cd00056; ENDO3c; 1.
DR   Gene3D; 1.10.1670.10; -; 1.
DR   Gene3D; 3.30.310.20; -; 1.
DR   InterPro; IPR037046; AlkA_N_sf.
DR   InterPro; IPR000035; Alkylbase_DNA_glycsylse_CS.
DR   InterPro; IPR011257; DNA_glycosylase.
DR   InterPro; IPR003265; HhH-GPD_domain.
DR   InterPro; IPR023170; HhH_base_excis_C.
DR   InterPro; IPR012904; OGG_N.
DR   Pfam; PF00730; HhH-GPD; 1.
DR   Pfam; PF07934; OGG_N; 1.
DR   SMART; SM00478; ENDO3c; 1.
DR   SUPFAM; SSF48150; SSF48150; 1.
DR   PROSITE; PS00516; ALKYLBASE_DNA_GLYCOS; 1.
PE   1: Evidence at protein level;
KW   DNA damage; DNA repair; Hydrolase; Reference proteome.
FT   CHAIN           1..303
FT                   /note="DNA-3-methyladenine glycosylase"
FT                   /id="PRO_0000194880"
FT   ACT_SITE        258
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   SITE            238
FT                   /note="Determinant for substrate specificity and/or
FT                   activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   303 AA;  35634 MW;  17BEEFC78457A591 CRC64;
     MTWHEVNDVI VITLPEIFDM NANLGYLTRE KNECMYEIEN NIITKVIAIG EIRSLVQVSV
     INNKQMIVQF LNDSRPVEQW KREEIVKYIH EWFDLDNDLT PFYEMAKADP LLKMPARKFY
     GLRVIGIPDL FEALCWGVLG QQINLAFAYS LKKQFVEAFG DSIEWNGKKY WVFPPYERIA
     RLTPTDLADI KMTVKKSEYI IGIARLMASG ELSREKLMKM NFKDAEKNLI KIRGIGPWTA
     NYVLMRCLRF PTAFPIDDVG LIHSIKILRN MNRKPTKDEI LEISVPWKEW QSYATFYLWR
     VLY